1Q57

The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-08
Detector	ADSC QUANTUM 315
Wavelength(s)	1.1000
Spacegroup name	P 1 21 1
Unit cell lengths	117.179, 171.567, 118.581
Unit cell angles	90.00, 99.86, 90.00

Refinement procedure

Resolution	20.000 - 3.450
R-factor	0.30077
Rwork	0.299
R-free	0.32600 *
Structure solution method	MAD + MIR
RMSD bond length	0.017
RMSD bond angle	1.898
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.1.80)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	116.800	3.570
High resolution limit [Å]	3.450	3.450
Rmerge	0.044 *	0.506 *
Number of reflections	60625
<I/σ(I)>	29.1	2.8
Completeness [%]	99.9	100
Redundancy	3.8	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6 *	4 *	MES, sodium citrate, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	MES	0.1 (M)	pH6.0
3	1	reservoir	sodium citrate	0.81-0.855 (M)